@article{citeulike:477493,
	title = {Epitope mapping analysis of apolipoprotein B-100 using a surface plasmon resonance-based biosensor.},
	address = {Institute of Mutagenesis and Differentiation, CNR, Area della Ricerca San Cataldo, 56100 Via Moruzzi, Ghezzano-Pisa, Italy. lel@imd.pi.cnr.it},
	author = {L. Laricchia Robbio and P. Uboldi and S. Marcovina and R. P. Revoltella and A. L. Catapano},
	journal = {Biosens Bioelectron},
	month = {December},
	number = {9-12},
	pages = {963--969},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=11679276},
	volume = {16},
	year = {2001},
	biburl = {http://www.bibsonomy.org/bibtex/264fee8a74054cacb021a4106ed8baf1f/biblio24},
	abstract = {Using a surface plasmon resonance (SPR)-based biosensor (BIA-technology), we have studied the interaction of ten different murine monoclonal antibodies (mAbs, all IgG(1)), raised against the main protein constituent of human low density lipoprotein (LDL), i.e. the apolipoprotein B-100 (apoB-100). These mAbs identify distinct domains on apoB-100, relevant to LDL-receptor interaction: epitopes in the amino-terminal region (mAbs L7, L9, L10 and L11: aa 1-1297) and in the middle region (mAb 6B: aa 1480-1693; mAbs 2A, 3B: aa 2152-2377; mAbs 9A, L2 and L4: aa 2657-3248) of native apoB-100. A multisite binding analysis was performed to further characterize the epitopes recognized by all these mAbs. A rabbit anti-mouse IgG(1)-Fc antibody (RAM.Fc) was first coupled to the gold surface in order to capture one anti-human apoB-100 mAb. ApoB-100 protein was subsequently injected and allowed to react with this immobilized, oriented antibody. Multisite binding assays were then performed, by sequentially flowing other mAbs, in different orders, over the sensing surface. The capacity of each mAb to interact with the entrapped apoB-100 in a multimolecular complex was monitored in real time by SPR. The results achieved were comparable to those obtained by western immunoblotting using the same reagents. However, SPR ensures a more detailed epitope identification, demonstrating that BIA-technology can be successfully used for mapping distinct epitopes on apoB-100 protein in solution dispensing with labels and secondary tracers; moreover, compared with conventional immunoassays, it is significantly time saving (CNR-P.F. MADESS 2).},
	issn = {0956-5663}, doi = {10.1016/S0956-5663(01)00244-5 }, comment = {lel@imd.pi.cnr.it/requested/wrong address
alberico.catapano@unimi.it/requested}, citeulike-article-id = {477493}, priority = {2},
	keywords = {apob epitope mapping spr }
}

@article{citeulike:477494,
	title = {Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction.},
	address = {Institute of Pharmacological Sciences, University of Milano, Italy.},
	author = {S. Fantappiè and A. Corsini and A. Sidoli and P. Uboldi and A. Granata and T. Zanelli and P. Rossi and S. Marcovina and R. Fumagalli and A. L. Catapano},
	journal = {Journal of Lipid Research},
	month = {August},
	number = {8},
	pages = {1111--1121},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=1279088},
	volume = {33},
	year = {1992},
	biburl = {http://www.bibsonomy.org/bibtex/28470a55ffd3031830371a1e0072d15bf/biblio24},
	abstract = {We have characterized the epitopes for ten murine monoclonal antibodies (Mabs) to human low density lipoprotein (LDL) and studied their ability to interfere with the LDL-receptor interaction. The epitopes for the antibodies were defined by using the following approaches: 1) interaction with apoB-48; 2) interaction with apoB-100 thrombolytic fragments; and 3) interaction with beta-galactosidase-apoB fusion proteins spanning different areas of the apoB-100 sequence. The results obtained are consistent with the following map of epitopes: Mab 6E, amino acids (aa) 1-1297, Mabs 5A and 6B, aa 1480-1693, Mabs 2A, 7A, 3B, and 4B, aa 2152-2377, Mabs 8A and 9A, aa 2657-3248 and 3H, aa 4082-4306. Four Mabs (2A, 5A, 7A, and 9A) whose epitopes are located in three different areas of apoB, dramatically reduced (up to 95%) the LDL-receptor interaction on cultured human fibroblasts; Fab fragments were as effective as the whole antibodies. Mab 3H, on the other hand, increased LDL binding up to threefold. These findings are consistent with the hypothesis that several areas of apoB-100 are involved independently or in concert in modulating the apoprotein B conformation required for interaction with the LDL receptor.},
	issn = {0022-2275}, citeulike-article-id = {477494}, priority = {2},
	keywords = {apob epitope mapping }
}

@article{citeulike:477517,
	title = {Immunoreactivity of apo B towards monoclonal antibodies that inhibit the LDL-receptor interaction: effects of LDL oxidation.},
	address = {Institute of Pharmacological Sciences, University of Milano, Italy.},
	author = {S. Negri and P. Roma and R. Fogliatto and P. Uboldi and S. Marcovina and A. L. Catapano},
	journal = {Atherosclerosis},
	month = {June},
	number = {1},
	pages = {37--41},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=7692863},
	volume = {101},
	year = {1993},
	biburl = {http://www.bibsonomy.org/bibtex/2acca9a5e11f5de28586667a664f1e859/biblio24},
	abstract = {We studied the immunochemical stability of the epitopes for six monoclonal antibodies to human apolipoprotein B-100 upon Cu(2+)-mediated (20 microM) oxidation of LDL. The antibodies used in this study, some of which are known to interfere with the interaction of LDL with their cellular receptors, recognize epitopes in the amino terminal region (Mb 19), in the middle part (6B, 2A, 7A, and 9A) and near aa 3500 (Mb 47) of native apo B. All antibodies except one (7A) recognized native and oxidized LDL (OxLDL) equally well; the immunoreactivity of the epitope for Ab 7A was markedly reduced upon LDL oxidation. Since antibodies 2A, 7A, 9A, and Mb 47 inhibit the LDL-receptor interaction and OxLDL poorly interact in vitro with the LDL receptor we conclude that: (1) various epitopes for monoclonal antibodies against native apo B are spared upon LDL oxidation; and (2) the epitopes for antibodies 2A, 9A, and Mb 47 do not define a unique domain of apo B directly involved in the binding of LDL to their receptor.},
	issn = {0021-9150}, doi = {10.1016/0021-9150(93)90099-G  }, citeulike-article-id = {477517}, priority = {2},
	keywords = {apob epitope mapping }
}